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Identification and primary structure of a calbindin 9K binding domain in the plasma membrane Ca 2+ pump
Author(s) -
James Peter,
Vorherr Thomas,
Thulin Eva,
Forsen Sture,
Carafoli Ernesto
Publication year - 1991
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(91)80106-d
Subject(s) - calmodulin , chemistry , linker , fluorescence , calbindin , membrane , biophysics , binding site , diaphragm pump , biochemistry , calcium , biology , enzyme , organic chemistry , nanotechnology , physics , materials science , quantum mechanics , micropump , computer science , operating system
Bovine calbindin 9K has been conjugated to a bifunctional, photoactivatable, cleavable and radioactive cross‐linker. It has been photolyzed in the presence of preparations of the purified crythrocyte Ca 2+ pump, and shown to interact with it in the presence of Ca 2+ . The affinity of the interaction has been studied using the fluorescence enhancement of dansylated calbindin 9K incubated with the synthetic calmodulin binding domain of the pump. Two versions of the domain have been used, one corresponding to its full length (28 residues), one to about of it (20 residues). The affinity of the interaction was between 5 and 10 times lower than in the case of calmodulin.